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The reconstituted 'humanized liver' in TK-NOG mice is mature and functional |
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| Authors: | Hasegawa Masami Kawai Kenji Mitsui Tetsuya Taniguchi Kenji Monnai Makoto Wakui Masatoshi Ito Mamoru Suematsu Makoto Peltz Gary Nakamura Masato Suemizu Hiroshi |
| Institution: | aDepartment of Chemistry, University of Oslo, PO Box 1033 Blindern, 0315 Oslo, Norway;bDepartment of Biochemistry, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Montebello, 0310 Oslo, Norway;cDepartment of Molecular Biosciences, University of Oslo, PO Box 1041 Blindern, 0316 Oslo, Norway;dGlyconor Mass Spectrometry, University of Oslo, Norway;eDepartment of Pharmaceutical Biosciences, School of Pharmacy, University of Oslo, PO Box 1068 Blindern, 0316 Oslo, Norway;fDepartment of Biological Chemistry, Medical School, University of Michigan, Ann Arbor, MI 48109-0606, USA;gCentre for Cancer Biomedicine, University of Oslo, Norway |
| Abstract: | The Marasmius oreades mushroom lectin (MOA) is well known for its exquisite binding specificity for blood group B antigens. In addition to its N-terminal carbohydrate-binding domain, MOA possesses a C-terminal domain with unknown function, which structurally resembles hydrolytic enzymes. Here we show that MOA indeed has catalytic activity. It is a calcium-dependent cysteine protease resembling papain-like cysteine proteases, with Cys215 being the catalytic nucleophile. The possible importance of MOA’s proteolytic activity for mushroom defense against pathogens is discussed. |
| Keywords: | Abbreviations: MalNEt N-ethylmaleimide MOA Marasmius oreades agglutinin PSL Polyporous squamosus lectin r m s d root mean square deviation |
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